Ornitin karbamoiltransferaza
| Ornitin karbamoiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Ornitin karbamoiltransferaza trimer, Human | |||||||||
| Identifikatori | |||||||||
| EC broj | 2.1.3.3 | ||||||||
| CAS broj | 9001-69-8 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Ornitin karbamoiltransferaza (EC 2.1.3.3, citrulinska fosforilaza, ornitinska transkarbamilaza, OTC, karbamilfosfat-ornitinska transkarbamilaza, L-ornitinska karbamoiltransferaza, L-ornitinska karbamiltransferaza, L-ornitinska transkarbamilaza, ornitinska karbamiltransferaza) je enzim sa sistematskim imenom karbamoil-fosfat:L-ornitin karbamoiltransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- karbamoil fosfat + L-ornitin fosfat + L-citrulin
Ovaj biljni enzim takođe katalizuje reakcije EC 2.1.3.6, putrescin karbamoiltransferaze, EC 2.7.2.2, karbamatne kinaze i EC 3.5.3.12 agmatinske deiminaze. On deluje kao putrescinska sintaza, koji konvertuje agmatin [(4-aminobutil)guanidin] i ornitin u putrescin i citrullin, respektivno.
Reference
- ↑ Bishop, S.H. and Grisolia, S. (1967). „Crystalline ornithine transcarbamylase”. Biochim. Biophys. Acta 139: 344-348. PMID 6034676.
- ↑ Marshall, M. and Cohen, P.P. (1972). „Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. I. Isolation and subunit structure”. J. Biol. Chem. 247: 1641-1653. PMID 4622303.
- ↑ Marshall, M. and Cohen, P.P. (1972). „Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for carbamyl-P and L-norvaline, correlation with steady state kinetics”. J. Biol. Chem. 247: 1654-1668. PMID 4622304.
- ↑ Marshall, M. and Cohen, P.P. (1972). „Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. 3. Effects of chemical modifications of specific residues on ligand binding and enzymatic activity”. J. Biol. Chem. 247: 1669-1682. PMID 4622305.
Literatura
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.
Spoljašnje veze
- MeSH Ornithine+carbamoyltransferase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
